1xtl

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[[Image:1xtl.gif|left|200px]]
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{{STRUCTURE_1xtl| PDB=1xtl | SCENE= }}
{{STRUCTURE_1xtl| PDB=1xtl | SCENE= }}
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'''Crystal structure of P104H mutant of SOD-like protein from Bacillus subtilis.'''
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===Crystal structure of P104H mutant of SOD-like protein from Bacillus subtilis.===
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==Overview==
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It is known that several prokaryotic protein sequences, characterized by high homology with the eukaryotic Cu,ZnSODs, lack some of the metal ligands. In the present work, we have stepwise reintroduced the two missing copper ligands in the SOD-like protein of Bacillus subtilis, through site-directed mutagenesis. The mutant with three out of the four His that bind copper is not active, whereas the fully reconstituted mutant displays an activity of about 10% that of human Cu,ZnSOD. The mutated proteins have been characterized in solution and in the solid state. In solution, the proteins experience conformational disorder, which is believed to be partly responsible for the decreased enzymatic activity and sheds light on the tendency of several human SOD mutants to introduce mobility in the protein frame. In the crystal, on the contrary, the protein has a well-defined conformation, giving rise to dimers through the coordination of an exogenous zinc ion. The catalytic properties of the double mutant, which might be regarded as a step in an artificial evolution from a nonactive SOD to a fully functioning enzyme, are discussed on the basis of the structural and dynamical properties.
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The line below this paragraph, {{ABSTRACT_PUBMED_16173759}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16173759 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16173759}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
From an inactive prokaryotic SOD homologue to an active protein through site-directed mutagenesis., Banci L, Benvenuti M, Bertini I, Cabelli DE, Calderone V, Fantoni A, Mangani S, Migliardi M, Viezzoli MS, J Am Chem Soc. 2005 Sep 28;127(38):13287-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16173759 16173759]
From an inactive prokaryotic SOD homologue to an active protein through site-directed mutagenesis., Banci L, Benvenuti M, Bertini I, Cabelli DE, Calderone V, Fantoni A, Mangani S, Migliardi M, Viezzoli MS, J Am Chem Soc. 2005 Sep 28;127(38):13287-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16173759 16173759]
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A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal., Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7541-6. Epub 2005 May 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15897454 15897454]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Superoxide dismutase mutant]]
[[Category: Superoxide dismutase mutant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:29:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:27:41 2008''

Revision as of 09:27, 27 July 2008

Image:1xtl.png

Template:STRUCTURE 1xtl

Crystal structure of P104H mutant of SOD-like protein from Bacillus subtilis.

Template:ABSTRACT PUBMED 16173759

About this Structure

1XTL is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

From an inactive prokaryotic SOD homologue to an active protein through site-directed mutagenesis., Banci L, Benvenuti M, Bertini I, Cabelli DE, Calderone V, Fantoni A, Mangani S, Migliardi M, Viezzoli MS, J Am Chem Soc. 2005 Sep 28;127(38):13287-92. PMID:16173759

A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal., Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7541-6. Epub 2005 May 16. PMID:15897454

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